ID C9ZPX8_TRYB9 Unreviewed; 632 AA.
AC C9ZPX8;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=TbgDal_V5960 {ECO:0000313|EMBL:CBH11456.1};
OS Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH11456.1, ECO:0000313|Proteomes:UP000002316};
RN [1] {ECO:0000313|Proteomes:UP000002316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316};
RX PubMed=20404998; DOI=10.1371/journal.pntd.0000658;
RA Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A.,
RA Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W.,
RA Barry J.D., Berriman M., Hertz-Fowler C.;
RT "The genome sequence of Trypanosoma brucei gambiense, causative agent of
RT chronic human african trypanosomiasis.";
RL PLoS Negl. Trop. Dis. 4:E658-E658(2010).
CC -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions. It is
CC composed of at least EIF4A, EIF4E and EIF4G.
CC {ECO:0000256|ARBA:ARBA00025917}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50
CC subfamily. {ECO:0000256|ARBA:ARBA00006517}.
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DR EMBL; FN554968; CBH11456.1; -; Genomic_DNA.
DR RefSeq; XP_011773743.1; XM_011775441.1.
DR AlphaFoldDB; C9ZPX8; -.
DR GeneID; 23861619; -.
DR KEGG; tbg:TbgDal_V5960; -.
DR VEuPathDB; TriTrypDB:Tbg972.5.5960; -.
DR OrthoDB; 1188at2759; -.
DR Proteomes; UP000002316; Chromosome 5.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd00268; DEADc; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR012562; GUCT.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08152; GUCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CBH11456.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 45..73
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 76..259
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 287..431
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..73
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 68786 MW; 00F97BEDF496D922 CRC64;
MSSRAEEGTH RHEGHVTKTK RSREEMTGNE ETDQEPNNGS AAVGRPFSEF NLSSGMVKAL
EAQGIVSLFP VQALTFEAIM RGEDVLVQAR TGSGKTLAFG IPIVEKLNKK EGPLARGRGP
AAVIFCPTRE LAIQVRDVLA GVSGDLVVAA LYGGVAYSTQ ERVLFSGVDI VVATPGRAKD
FLEKGTLHFE RVKMVCLDEA DHMLDIGFKE DIELLLQRVA EQNGSTPDEP KHQTLLFSAT
VPDWVHTCSF ISKNKKFIDM VGQGAMRAAN TIRFYRRKCG FAEVSSMLAD LVKVYSGRHG
RTLIFTNTKK DCHDLSINNT KLDSQCLHGD MQQEQRESTM KSFRDNKFSV LIATDVAARG
LDLPMVDLVI QCAPPTDIDA FIHRAGRTGR AGRKGVCVLL HQPKDEYVVE RIERHAKIKF
EVLPAPTREE ILKAVARDAA EDMARVERSA TNLFMDQAAE LLKDADPTEI LASAIAVMSG
YTSSITKRGL ISGARGSATV QMLGQRSLPT HVFCSILRNN LGDELFMRCR DITLLQDAPG
CVFDVPEDVV DRILNTPVQG MELSVIETLP PIIARELNSG SRGNRGGGGG GGGYRGGPRG
GGYNQYNRNG GGGGGGGGRS WGSGYRSTQR RY
//
